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Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay
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| Zeitschriftentitel: | Clinical and Vaccine Immunology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Clinical and Vaccine Immunology, 15, 2008, 3, S. 402-411 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko |
|---|---|
| author |
Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko |
| spellingShingle |
Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko Clinical and Vaccine Immunology Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy |
| author_sort |
zhang, chunbin |
| spelling |
Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko 1556-6811 1556-679X American Society for Microbiology Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy http://dx.doi.org/10.1128/cvi.00366-07 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Ehrlichia ewingii</jats:italic> , a tick-transmitted rickettsia previously known only as a canine pathogen, was recently recognized as a human pathogen. <jats:italic>E. ewingii</jats:italic> has yet to be cultivated, and there is no serologic test available to diagnose <jats:italic>E. ewingii</jats:italic> infection. Previously, a fragment (505 bp) of a single <jats:italic>E. ewingii</jats:italic> gene homologous to 1 of 22 genes encoding <jats:italic>Ehrlichia chaffeensis</jats:italic> immunodominant major outer membrane proteins 1 (OMP-1s)/P28s was identified. The purposes of the present study were to (i) determine the <jats:italic>E. ewingii omp-1</jats:italic> gene family, (ii) determine each OMP-1-specific peptide, and (iii) analyze all OMP-1 synthesized peptides for antigenicity. Using nested touchdown PCR and a primer walking strategy, we found 19 <jats:italic>omp-1</jats:italic> paralogs in <jats:italic>E. ewingii</jats:italic> . These genes are arranged in tandem downstream of <jats:italic>tr1</jats:italic> and upstream of <jats:italic>secA</jats:italic> in a 24-kb genomic region. Predicted molecular masses of the 19 mature <jats:italic>E. ewingii</jats:italic> OMP-1s range from 25.1 to 31.3 kDa, with isoelectric points of 5.03 to 9.80. Based on comparative sequence analyses among OMP-1s from <jats:italic>E. ewingii</jats:italic> and three other <jats:italic>Ehrlichia</jats:italic> spp., each <jats:italic>E. ewingii</jats:italic> OMP-1 oligopeptide that was predicted to be antigenic, bacterial surface exposed, unique in comparison to the other <jats:italic>E. ewingii</jats:italic> OMP-1s, and distinct from those of other <jats:italic>Ehrlichia</jats:italic> spp. was synthesized for use in an enzyme-linked immunosorbent assay. Plasmas from experimentally <jats:italic>E. ewingii</jats:italic> -infected dogs reacted significantly with most of the OMP-1-specific peptides, indicating that multiple OMP-1s were expressed and immunogenic in infected dogs. The results support the utility of the tailored OMP-1 peptides as <jats:italic>E. ewingii</jats:italic> serologic test antigens. </jats:p> Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in <i>Ehrlichia ewingii</i> for Use in a Serodiagnostic Assay Clinical and Vaccine Immunology |
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American Society for Microbiology, 2008 |
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Clinical and Vaccine Immunology |
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| title |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_unstemmed |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_full |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_fullStr |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_full_unstemmed |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_short |
Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_sort |
identification of 19 polymorphic major outer membrane protein genes and their immunogenic peptides in
<i>ehrlichia ewingii</i>
for use in a serodiagnostic assay |
| topic |
Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy |
| url |
http://dx.doi.org/10.1128/cvi.00366-07 |
| publishDate |
2008 |
| physical |
402-411 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
<jats:italic>Ehrlichia ewingii</jats:italic>
, a tick-transmitted rickettsia previously known only as a canine pathogen, was recently recognized as a human pathogen.
<jats:italic>E. ewingii</jats:italic>
has yet to be cultivated, and there is no serologic test available to diagnose
<jats:italic>E. ewingii</jats:italic>
infection. Previously, a fragment (505 bp) of a single
<jats:italic>E. ewingii</jats:italic>
gene homologous to 1 of 22 genes encoding
<jats:italic>Ehrlichia chaffeensis</jats:italic>
immunodominant major outer membrane proteins 1 (OMP-1s)/P28s was identified. The purposes of the present study were to (i) determine the
<jats:italic>E. ewingii omp-1</jats:italic>
gene family, (ii) determine each OMP-1-specific peptide, and (iii) analyze all OMP-1 synthesized peptides for antigenicity. Using nested touchdown PCR and a primer walking strategy, we found 19
<jats:italic>omp-1</jats:italic>
paralogs in
<jats:italic>E. ewingii</jats:italic>
. These genes are arranged in tandem downstream of
<jats:italic>tr1</jats:italic>
and upstream of
<jats:italic>secA</jats:italic>
in a 24-kb genomic region. Predicted molecular masses of the 19 mature
<jats:italic>E. ewingii</jats:italic>
OMP-1s range from 25.1 to 31.3 kDa, with isoelectric points of 5.03 to 9.80. Based on comparative sequence analyses among OMP-1s from
<jats:italic>E. ewingii</jats:italic>
and three other
<jats:italic>Ehrlichia</jats:italic>
spp., each
<jats:italic>E. ewingii</jats:italic>
OMP-1 oligopeptide that was predicted to be antigenic, bacterial surface exposed, unique in comparison to the other
<jats:italic>E. ewingii</jats:italic>
OMP-1s, and distinct from those of other
<jats:italic>Ehrlichia</jats:italic>
spp. was synthesized for use in an enzyme-linked immunosorbent assay. Plasmas from experimentally
<jats:italic>E. ewingii</jats:italic>
-infected dogs reacted significantly with most of the OMP-1-specific peptides, indicating that multiple OMP-1s were expressed and immunogenic in infected dogs. The results support the utility of the tailored OMP-1 peptides as
<jats:italic>E. ewingii</jats:italic>
serologic test antigens.
</jats:p> |
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| author | Zhang, Chunbin, Xiong, Qingming, Kikuchi, Takane, Rikihisa, Yasuko |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Ehrlichia ewingii</jats:italic> , a tick-transmitted rickettsia previously known only as a canine pathogen, was recently recognized as a human pathogen. <jats:italic>E. ewingii</jats:italic> has yet to be cultivated, and there is no serologic test available to diagnose <jats:italic>E. ewingii</jats:italic> infection. Previously, a fragment (505 bp) of a single <jats:italic>E. ewingii</jats:italic> gene homologous to 1 of 22 genes encoding <jats:italic>Ehrlichia chaffeensis</jats:italic> immunodominant major outer membrane proteins 1 (OMP-1s)/P28s was identified. The purposes of the present study were to (i) determine the <jats:italic>E. ewingii omp-1</jats:italic> gene family, (ii) determine each OMP-1-specific peptide, and (iii) analyze all OMP-1 synthesized peptides for antigenicity. Using nested touchdown PCR and a primer walking strategy, we found 19 <jats:italic>omp-1</jats:italic> paralogs in <jats:italic>E. ewingii</jats:italic> . These genes are arranged in tandem downstream of <jats:italic>tr1</jats:italic> and upstream of <jats:italic>secA</jats:italic> in a 24-kb genomic region. Predicted molecular masses of the 19 mature <jats:italic>E. ewingii</jats:italic> OMP-1s range from 25.1 to 31.3 kDa, with isoelectric points of 5.03 to 9.80. Based on comparative sequence analyses among OMP-1s from <jats:italic>E. ewingii</jats:italic> and three other <jats:italic>Ehrlichia</jats:italic> spp., each <jats:italic>E. ewingii</jats:italic> OMP-1 oligopeptide that was predicted to be antigenic, bacterial surface exposed, unique in comparison to the other <jats:italic>E. ewingii</jats:italic> OMP-1s, and distinct from those of other <jats:italic>Ehrlichia</jats:italic> spp. was synthesized for use in an enzyme-linked immunosorbent assay. Plasmas from experimentally <jats:italic>E. ewingii</jats:italic> -infected dogs reacted significantly with most of the OMP-1-specific peptides, indicating that multiple OMP-1s were expressed and immunogenic in infected dogs. The results support the utility of the tailored OMP-1 peptides as <jats:italic>E. ewingii</jats:italic> serologic test antigens. </jats:p> |
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| spelling | Zhang, Chunbin Xiong, Qingming Kikuchi, Takane Rikihisa, Yasuko 1556-6811 1556-679X American Society for Microbiology Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy http://dx.doi.org/10.1128/cvi.00366-07 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Ehrlichia ewingii</jats:italic> , a tick-transmitted rickettsia previously known only as a canine pathogen, was recently recognized as a human pathogen. <jats:italic>E. ewingii</jats:italic> has yet to be cultivated, and there is no serologic test available to diagnose <jats:italic>E. ewingii</jats:italic> infection. Previously, a fragment (505 bp) of a single <jats:italic>E. ewingii</jats:italic> gene homologous to 1 of 22 genes encoding <jats:italic>Ehrlichia chaffeensis</jats:italic> immunodominant major outer membrane proteins 1 (OMP-1s)/P28s was identified. The purposes of the present study were to (i) determine the <jats:italic>E. ewingii omp-1</jats:italic> gene family, (ii) determine each OMP-1-specific peptide, and (iii) analyze all OMP-1 synthesized peptides for antigenicity. Using nested touchdown PCR and a primer walking strategy, we found 19 <jats:italic>omp-1</jats:italic> paralogs in <jats:italic>E. ewingii</jats:italic> . These genes are arranged in tandem downstream of <jats:italic>tr1</jats:italic> and upstream of <jats:italic>secA</jats:italic> in a 24-kb genomic region. Predicted molecular masses of the 19 mature <jats:italic>E. ewingii</jats:italic> OMP-1s range from 25.1 to 31.3 kDa, with isoelectric points of 5.03 to 9.80. Based on comparative sequence analyses among OMP-1s from <jats:italic>E. ewingii</jats:italic> and three other <jats:italic>Ehrlichia</jats:italic> spp., each <jats:italic>E. ewingii</jats:italic> OMP-1 oligopeptide that was predicted to be antigenic, bacterial surface exposed, unique in comparison to the other <jats:italic>E. ewingii</jats:italic> OMP-1s, and distinct from those of other <jats:italic>Ehrlichia</jats:italic> spp. was synthesized for use in an enzyme-linked immunosorbent assay. Plasmas from experimentally <jats:italic>E. ewingii</jats:italic> -infected dogs reacted significantly with most of the OMP-1-specific peptides, indicating that multiple OMP-1s were expressed and immunogenic in infected dogs. The results support the utility of the tailored OMP-1 peptides as <jats:italic>E. ewingii</jats:italic> serologic test antigens. </jats:p> Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in <i>Ehrlichia ewingii</i> for Use in a Serodiagnostic Assay Clinical and Vaccine Immunology |
| spellingShingle | Zhang, Chunbin, Xiong, Qingming, Kikuchi, Takane, Rikihisa, Yasuko, Clinical and Vaccine Immunology, Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay, Microbiology (medical), Clinical Biochemistry, Immunology, Immunology and Allergy |
| title | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_full | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_fullStr | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_full_unstemmed | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_short | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| title_sort | identification of 19 polymorphic major outer membrane protein genes and their immunogenic peptides in <i>ehrlichia ewingii</i> for use in a serodiagnostic assay |
| title_unstemmed | Identification of 19 Polymorphic Major Outer Membrane Protein Genes and Their Immunogenic Peptides in Ehrlichia ewingii for Use in a Serodiagnostic Assay |
| topic | Microbiology (medical), Clinical Biochemistry, Immunology, Immunology and Allergy |
| url | http://dx.doi.org/10.1128/cvi.00366-07 |